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SciPoultryAndMeatProcessing - Barbut - 13 Meat Processing - v01 PDF
SciPoultryAndMeatProcessing - Barbut - 13 Meat Processing - v01 PDF
PRINCIPLES OF MEAT
PROCESSING
The Science of
Poultry and Meat Processing
Shai Barbut PhD University of Guelph
Chapters
1. AUTOMATION
2. GLOBAL PERSPECTIVE
3. STRUCTURE* AND MUSCLE PHYSIOLOGY
4. LIVE BIRD HANDLING*
5. PRIMARY PROCESSING OF POULTRY*
6. HACCP IN PRIMARY PROCESSING*
7. INSPECTION AND GRADING*
8. STUNNING*
9. PORTIONING, DEBONING AND FRESH MEAT
COMPOSITION*
10. FURTHER PROCESSING – EQUIPMENT
11. HEAT PROCESSING, COOLING AND PRESERVATION
METHODS
12. HACCP IN COOKED MEAT OPERATIONS
13. PRINCIPLES OF MEAT PROCESSING
14. BATTERING AND BREADING – PRODUCTION UNDER
HACCP
15. MICROBIOLOGY AND SANITATION
16. EVALUATING TEXTURE AND SENSORY ATTRIBUTES
17. EVALUATING WATER/FAT BINDING AND COLOUR
18. WASTE TREATMENT AND BY-PRODUCTS
* Topics focussing on poultry. Rest of the chapters are related to both red meat and poultry.
Preface
The aim of The Science of Poultry and Meat Processing book is to provide students
and industry personnel with a comprehensive view of the modernized primary poultry
meat industry and further processing of both red meat and poultry. An emphasis is
placed on basic concepts as well as recent advancements such as automation (e.g.
increasing poultry line speed from 3,000 to 13,000 birds per hour over the last 40
years) and food safety (e.g. HACCP in primary and the further processing areas). The
book also includes chapters explaining basic muscle biology, protein gelation, heat
and mass transfer, microbiology, as well as meat colour and texture to help the reader
understand the underlying scientific concepts of meat processing. The Science of
Poultry and Meat Processing book is based on over two decades of university teaching
experiences, and is designed to be used as a course textbook by students, as well as a
resource for professionals working in the food industry. The book is available online,
at no cost, to any interested learner. Using this format has also allowed me to include
many colour pictures, illustrations and graphs to help the reader.
ii
The book is dedicated to my past and current students who have inspired me to
learn more and conduct challenging research projects. I see this as an opportunity to
give back to the field that I have received so much from as a student and as a faculty
member. Looking back, I have learned a great deal from my MSc and PhD advisor,
Dr. A. Maurer, who was the student of Dr. R. Baker - the father of poultry processing
in North America. I would also like to thank Dr. H. Swatland with whom I worked for
almost 20 years, for the many challenging scientific discussions.
Writing The Science of Poultry and Meat Processing book was a long process, which
also included having all chapters peer reviewed. I appreciate the help of my colleagues,
but I still take responsibility for any inaccuracy in the book. If you have comments or
suggestions, I would appreciate hearing from you (sbarbut@uoguelph.ca), as I am
planning to revise and update a few chapters on a yearly basis.
I would like to thank the many people who have helped me during the writing process.
To Deb Drake who entered all of the material for the book, to Mary Anne Smith who
assisted in editing, and to ArtWorks Media for the design and desktop publishing
of the book. I greatly appreciate the help of my colleagues who reviewed chapters
and provided useful discussions. They include Mark B., Ori B., Sarge B., Gregoy
B., Joseph C., Mike D., Hans G., Theo H., Melvin H., Myra H., Walter K., Roland
K., Anneke L., Massimo M., Johan M., Erik P., Robert R., Uwe T., Rachel T., Jos
V., Keith W., and Richard Z. I would also like to thank my family for their love and
support during the entire process.
iii
© 2015 Shai Barbut
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13.1 Introduction
the market was mainly set for selling whole birds and some bone-in cut up parts).
It also resulted in the introduction of mechanical deboning of the meat left on the
frames. All these developments created a market for various innovative further
processed meat products (Table 13.1.1; Fig. 13.1.1). Overall, this is an example
of the industry successfully responding to consumer demand for more convenient
food items including semi and fully prepared items. In this case, the increase in
poultry meat consumption (Chapter 2) has been the result of aggressive marketing,
the meat’s favorable nutrient profile, and its competitive price. As discussed in this
book, these developments have been coupled with the introduction of automation,
computer assisted programming (e.g., see discussion on Least Cost Formulation
below), and increasing line speed.
Table 13.1.1 Categories of the major meat/poultry further processed products on the international
market. Note: smoking procedures and cooking recipes for most products are
provided at the end of the chapter.
Overall, meat and meat products are mainly composed of protein, water, fat,
minerals (salts), and some carbohydrates. Proteins represent the major building
blocks of meat products and a major section in this chapter is devoted to protein
gelation. Mezzenga and Fischer (2013) indicated that protein aggregation has
fundamental relevance not only in the food industry (e.g., providing texture to meat
products, gelation of yogurt) but also in the medical field (blood coagulation by
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-3
Figure 13.1.2 Schematic representation of the physical description of proteins in soft condensed
Figure 13.1.1 Examples of different products. Showing chicken roast, turkey roast, turkey
matter. (a) A hypothetical unfolded protein, interpreted as an ampholytic
pepperoni sticks,
polyelectrolyte, poultry wieners,
containing both turkey
positivehamand
and negative
turkey bacon.
charges. (b) The
intermediate case ofPhoto by obtained
gelatin, Barbut andby Jinde.
hydrolysis of the triple-helical collagen:
the α-helical structure of gelatin strands can melt by increasing the temperature
and reversibly re-constitute upon cooling, with α-helices interacting to induce
gelation of the solution. (c) A folded globular protein, such as β-lactoglobulin,
In the food industry,
viewed astemperature canwith
a colloidal sphere range from
positive and0negative
– 300ºC, pHonfrom
charges 1 – 10,
its surfaces.
From Mezzenga and Fisher (2013).
and ionic strength spans as many as seven orders of magnitude. Food systems
consist of complex mixtures of various proteins, fats, carbohydrates, and salts. In
general, food proteins can be divided into different classes based on the amino acid
sequence and thermal history. The protein structure may be referred to as either
globular or random coil (folded or unfolded, respectively, Fig. 13.1.2). They will
be discussed in more detail later in the chapter.
94
13-4 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Figure 13.1.2 Schematic representation of the physical description of proteins in soft condensed
Figure 13.4.1 Effect of NaCl on the shrinking of cooked chicken muscle (700C) inmatter. the presence
(a) A hypothetical unfolded protein, interpreted as an ampholytic polyelectrolyte, containing both
of salt and different polyphosphates (0.5%). HMP – hexa meta phosphate;
positive and negative charges. (b) The intermediate case of gelatin, obtained by hydrolysis of
TPP –
tri poly phosphate; KENA – commercial phosphate blend; PP pyro
the triple-helical collagen: the α-helical structure of gelatin strands can melt by increasing the phosphate
(sodium acid).
temperature Redrawn
and reversibly from upon
re-constitute Shults andwith
cooling, Wierbicki (1973). to induce
α-helices interacting
0
gelation of the solution. (c) A folded globular protein, such as β-lactoglobulin, viewed as
a colloidal sphere with positive and negative charges on its surfaces. 1
35
From Mezzenga and Fisher (2013). 2
30 HMP 3
NO PHOSPHATES 4
25 TPP 5
KENA 6
13.2
20 Processing Categories of Meat Products PP 7
8
15
There is a vast array of meat products available for customers in the supermarket 9
today.
10 Table 13.1.1 shows examples of the main processing categories/groups,10
but overall there are hundreds of products available on the market, which can be
5
challenging for consumers to understand. To assist them, various systems have
been
0 suggested for classifying meat products. For example, one system groups
products
0 based
1 on2 their
3 preparation
4 5 method
6 7(Aberle
8 et9al., 2012)
10 and includes six
processing categories/groups: % NaCl IN MEAT
It should also be mentioned that new technologies have helped to diversify the
type of meat products we consume, especially the restructured meat products
(e.g., surimi), where small pieces of meat are made into a whole muscle/steak-
like product. This can be done by high speed flaking of partially frozen pieces of
meat (usually from tougher cuts) that are later recombined under pressure with
the addition of hydrocolloid gums (e.g., alginate with a calcium supplement).
The surimi technology is based on using minced chicken/fish meat, which is first
washed (to remove pigments and enzymes) and later extruded to create a muscle-
like fibrous structure and texture.
Section 13.2.1 further discusses the categories of meat products mentioned in Table
13.1.1 and provides an introduction to the unique characteristics of each category.
This is followed by an explanation of meat and non-meat ingredients used by
the industry (Section 13.3 and 13.4, respectively), protein gel matrix formation
(Section 13.5), meat emulsions (Section 13.6), casings (Section 13.7), and recipes
for twenty popular, high volume meat products produced by the industry (Section
13.8).
Some of the largest whole muscle products produced by the industry are a whole
ham and a whole oven roasted turkey breast portion (with or without smoke). This
is considered a premium product because it is produced from one intact muscle
portion. A brine solution (i.e., water, salt, spices, and often gums) is injected into the
raw product prior to smoking and cooking. A formula and preparation procedure
for this product are provided at the end of the chapter. This specific formulation
calls for the addition of 30% brine, but some products on the market are produced
with a 50% brine injection, which still results in a high protein level of about 14%.
The brine in this case is injected directly into the large diameter product, but in
the case of small diameter meat pieces it can be added by tumbling (see Chapter
10). In the case of a whole turkey breast, the meat is massaged or tumbled after
brine injection to assist in moisture absorption and help distribute the non-meat
ingredients within the muscle. The latter is important in the processing of any meat
product as an uneven distribution of ingredients can cause serious flavour, colour
and texture problems. Starches and hydrocolloid gums (e.g., carrageenans, see
13-6 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Section 13.4) are often added to assist in holding the injected brine. Non-meat
proteins such as soy concentrate/isolate and whey proteins can also be added
for the same purpose (see the recipe at the end of the chapter). The turkey breast
muscle can then be placed in a cooking bag or netting (with or without skin) and
smoked and cooked in a smokehouse until an internal temperature of at least 71°C
is reached.
b. Restructured Products
Poultry rolls can be made from dark meat, white meat, or their combination.
The meat portions/trimmings can be obtained from the breast, leg, skin, and
mechanically deboned meat (e.g., from poultry, beef, pork). In this product, pieces
of muscle tissue ranging in size from 5 – 25 cm are ‘glued’ together to form a
coherent product. This is done with the help of salt, which is used to extract the salt
soluble proteins such as actin and myosin (see previous chapters). During mixing,
these proteins form a tacky coating on the surfaces of the meat pieces. Later, during
cooking they coagulate and the ‘glue’ is set (similar to the phenomenon seen in a
liquid scrambled egg mix turning into an elastic structure during heating). These
proteins also contribute to moisture and fat holding within the cooked product, as
will be explained later in the chapter. Fat, skin and trimmings are usually finely
chopped (the term “emulsified” is often used by the industry, even though no
true emulsion is formed) and used to fill the voids between the larger pieces of
meat. Moisture is added to compensate for cooking losses and to improve the
juiciness of the product. If added moisture exceeds a certain fraction of the raw
meat (regulations vary by country), then the product must be labeled accordingly.
The meat and non-meat ingredients are then mixed together until the meat batter
becomes sticky (an indicator of good protein extraction) and all the added moisture
is absorbed. Next, the mix is placed in molds or stuffed into casings and the
product is cooked either in water (moisture-proof casings) or an oven (moisture-
and smoke-permeable casings), depending on market preference and equipment
availability.
placed in molds (e.g., 4 × 4” ham molds) or stuffed into large diameter fibrous
casings that determine the shape and size of the final product (see Section 13.7).
Then the product is smoked and cooked to at least 71°C. If moisture-proof casings
or metal molds are used, smoke flavourings can be added to the raw meat batter.
c. Ground Products
Hot dogs, frankfurters, and bologna are examples of emulsified meat products,
where the product has been finely chopped and results in a very homogenous
appearance. Dark leg meat, trimmings, skin, and/or mechanically deboned meat
are commonly used as the starting materials. The meat is then chopped in a bowl
chopper or an emulsion mill (see Chapter 10), which efficiently minces the meat
particles and emulsifies the fat (i.e., significantly reduces their size and helps
coat the small fat globules with proteins; see further explanation below). Salt is
used to extract the meat proteins, which are essential in binding the small meat
particles and stabilizing the fat globules within the protein matrix (Youssef and
Barbut, 2011; Barbut and Findlay, 1989). Nitrite is added to prevent Clostridium
botulinum growth and provide the typical cured meat colour (Chapters 15 and
16). The meat batter used for small (hot dogs, frankfurters) and large (Bologna)
diameter products and is stuffed into cellulose casings, smoked, and cooked in
a smokehouse. A newer process is the fully automated co-extrusion casing
application, where semi-liquid casing material is extruded onto the meat product as
it comes out of the stuffing machine. In this case, an edible casing such as collagen
or alginate is applied (see Chapter 10), which does not need to be removed prior
to packaging like cellulose casings would. This also helps reduce the potential for
cross contamination (e.g., Listeria), as product handling by workers is minimized.
Since frankfurters are such a popular item, a number of large processors have
constructed dedicated lines to continuously make this product (24/7). As with
other meat products, low microbial contamination and refrigeration temperatures
are essential to the safety and shelf life of these products (some manufacturers
guarantee a shelf life of over sixty days).
e. Coated Products
This category includes bone in and boneless products such as poultry drumsticks
and wings. The products can be coated with batter and breading (e.g., chicken
nuggets) or with a marinade (e.g., honey garlic sauce, BBQ mesquite sauce; see
recipes at the end of the chapter) for a few hours prior to cooking to increase
juiciness and yield of the fresh meat. The addition of moisture, salt, and spices
helps to compensate for evaporation losses during cooking and enhances the
flavour and texture of the meat. Coating systems, which include battering and
breading, are described in Chapter 14. Chicken nuggets, first introduced in the
1970s, are one of the most successful poultry products. The product was originally
prepared from a single piece of slightly marinated breast meat that was battered
and breaded. Later, nuggets made from trimmings (including white meat, dark
meat, skin, mechanically deboned meat and their combinations) appeared on the
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-9
market. These nuggets are usually prepared by marinating and mixing the meat
pieces with a brine solution. The meat is then formed into the desired shape,
battered, breaded and deep fat fried. Frying preserves the product shape, ‘cements’
the batter and breading to the product, and provides the typical crunchy texture.
Today there is a great emphasis on flexibility and traceability, where all data
can be kept on file electronically for a program such as HACCP (see Chapters
6 and 12). This is obviously another example of employing automation in the
meat industry to help streamline processes, reduce labour costs, and save money.
Overall, it should be recognized that computer programming of LCF requires
more basic information on ingredient composition (e.g., chemical composition,
bind value, water and fat holding capacity values), as well as skilled personnel to
operate computers and laboratory equipment. Meat technologists working in the
industry need to understand foundational scientific principles such as emulsion
stabilization and the functional properties of raw materials. This has become far
more important as the number of non-meat ingredients has increased (e.g., dozens
of different modified starches are now available on the market). It is important to
characterize the ingredients and establish ‘constants’ that can be used to optimize
the quality of the finished product. Two important examples are the bind value and
the emulsification capacity value that had to be initially established for running the
LCF programs.
Dr. Robert Saffle is generally credited with introducing the concept of meat
constants in the early 1960s (LaBudde and Lanier, 1995). The constants were
developed based on the meat emulsion stability test and were needed to develop
sausage LCF programs. Linear programming requires numerical values that
describe each meat’s specific properties in order to develop the best combination
of raw materials from the few dozen meat cuts/trims available each day to a typical
processor. The program’s goal is to calculate the best combination of ingredients
after satisfying requirements set by the operator. As mentioned previously, the
requirements can include protein, fat, and moisture content (Pearson and Tauber,
1984), as well as colour and meat bind values. It is important to note that when
Saffle developed his ‘constant’ emulsification value, at least one major North
American company had already developed its own criteria for evaluating meat.
Saffle’s constant emulsification values were generally based on multiplying the
percent salt soluble proteins in a certain cut of meat by the emulsifying capacity
results. Today, various medium and large companies continue to use Saffle’s values
in one form or another, whereas some large meat companies have developed their
own proprietary criteria for rating meats and use these values in their in-house
developed LCF programs.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-11
To simplify the discussion, non-meat ingredients can be divided into several major
groups including water, salts, spices, binders, and fillers.
Limits are imposed on the addition of several non-meat ingredients. The maximum
amounts permitted can be found in local regulations/meat inspection guides. An
example of a restricted ingredient is nitrite, which is added to prevent the growth
of deadly C. botulinum. At high levels, however, nitrite can present a health
hazard and therefore the level is tightly controlled (e.g., 120-200 ppm in USA and
Canada). Other functional ingredients, such as soy protein, are also commonly
regulated. For example, up to 3.5% soy can be added, alone or in combination with
other binders, to a variety of cooked sausages produced in the USA, However, if
this limit is exceeded, the product name must include the words “soy added” or
“imitation” to inform the consumer. In most countries, all the ingredients added
to a food/meat product must be listed on the label. Below is an example of an
ingredient list of a Canadian product showing the additives in a descending order
by weight:
The names and functions of most common non-meat additives used by the meat
industry are discussed below:
13-12 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
b. Salt – various salts can be added to meat products. The most common salt is table
salt (sodium chloride), which is used as a flavouring agent, protein solubilization
agent, and anti-microbial agent. Phosphates are another group of salts used to help
with meat protein extraction and solubilization (e.g., sodium tri-polyphosphate
is used to help extract myosin and actin). Other salts include sodium nitrite (for
preservation) and curing accelerators such as sodium erythorbate and sodium
ascorbate.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-13
b1. Sodium chloride (NaCl) is the most common ingredient added to meat
products because of its three major contributions:
1. S
odium chloride provides a distinct salty flavour, which makes a
substantial contribution when added to processed food. The classic
salty taste is represented by NaCl and lithium chloride (LiCl), whereas
other salts usually have additional flavours associated with them that
can include a mixture of sweet, bitter, sour, and salty. Chemically, it
appears that cations cause salty tastes, whereas anions inhibit salty tastes
(Sebranek and Bacus, 2007).
Among the anions, Cl– is the least inhibitory to the salty taste and does
not possess a taste of its own. Some anions can not only inhibit the taste
of their associated cations, but also contribute tastes of their own. An
example is the soapy taste associated with certain phosphates, which
results from the specific taste elicited by their anion.
In general, the most accepted model for describing the mechanism for
salty taste perception involves the interaction of hydrated cation-anion
complexes with the Shallenberger and Acree AH/B-type receptor site.
The individual structures of such complexes vary substantially. In the
presence of water, OH groups and salt anions/cations are associated with
specific receptor sites. Bitterness in salts involves a different receptor
mechanism that seems to be related to the sum of the ionic diameters of
the anion and cation components of the salt. Salts with ionic diameters
below 6.5 Å are salty in taste (LiCl = 4.98 Å, NaCl = 5.56 Å, KCl = 6.28
Å), although some individuals find KCl somewhat bitter. As the ionic
diameter increases (CsCl = 6.96 Å, CsI = 7.74 Å, MgCl2 = 8.50 Å), salts
become increasingly bitter.
In any case, a processor should always try to use the highest quality
salt possible. High quality refers to low levels of impurities (e.g., heavy
metals such as copper, iron). These trace contaminants are known as pro-
oxidants and can trigger fast lipid oxidation during storage, as will be
discussed later in the chapter when antioxidants are introduced.
2. S
odium chloride is involved in the protein extraction of the salt soluble
fraction (mainly myosin and actin; see also Chapter 3), which is very
important in the production of processed meat products as these proteins
can bind meat pieces/chunks when heated. Overall, extracting the
proteins and bringing them to the surface provides sticky surfaces on the
13-14 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
raw muscle cuts. These proteins also help bind moisture (i.e., increasing
the water holding capacity, WHC), assist in emulsifying fat particles in
comminuted products (by coating the fat globules), and increasing the
raw meat batter viscosity. Later, these extracted proteins coagulate and
bind both the meat particles (important for holding the product together)
and moisture (important to minimize cooking losses) to form a coherent
matrix that is important for texture as well as fat retention during heat
processing.
3. S
odium chloride suppresses microbial growth, as many microorganisms
are sensitive to high salt levels. High salt concentration can stop or
substantially slow the growth of microorganisms. In the past, high salt
levels (10 to 20%) were used as the main means of preservation because
these levels can provide shelf-stable meat products. This technique is
still used in places where refrigeration is a challenge and/or where the
traditional heavily salted products are preferred (i.e., the very high salt
content has to be washed out before consumption). However in many
markets today, substantially lower salt levels are used (e.g., 1.0 to 2.5%),
and it is only in conjunction with other additives (e.g., nitrite, lactic acid)
and appropriate refrigerated storage that product safety can be ensured
(Barbut and Findlay, 1989; Sebranek and Bacus, 2007).
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-15
b2. Sodium Nitrite (NaNO2) and Sodium Nitrate (NaNO3) – also known as
curing salts, are added at very low levels (usually 120-200 ppm in the USA) and
have four main functions.
2. C
ontribute to the development of the typical pink cured meat colour.
Again, the active compound is NO. This pink colour is very different
from the brown colour of a cooked product such as chicken leg meat,
turkey thigh, pork chop, or pork loin. This can be described as the
difference between a home-cooked pork chop and a cured pork ham (see
additional discussion in Chapter 16). The chemical reaction involved is:
3. P
rotect against lipid oxidation. Nitrite has antioxidant capabilities that
can help prolong the shelf life of meat products.
4. A
dds some flavour. Nitrite addition results in the development of certain
unique flavour notes.
b3. Phosphates – salts of phosphoric acid can work together with sodium
chloride to enhance muscle protein extraction, which in turn improves the water
holding capacity and reduces shrinkage during cooking (Fig. 13.4.1). There are
different types of phosphates available on the market. Examples of common
polyphosphates and orthophosphates in meat products are shown in Figure 13.4.2.
Alkaline polyphosphates such as tripolyphosphate (TPP) are the most popular and
by some estimates account for about 80% of the phosphates used by the meat
industry. Phosphate use is limited to 0.5% in the finished product in countries such
as the USA. This limit is mainly imposed to restrict water addition but greater
levels can also result in off flavour problems such as metallic or soapy as reported
by consumers. In countries such as Germany, the use of phosphate is not permitted
in several products.
The effects of using 0.5% TPP, pyrophosphate, and a commercial blend called
KENA (which contains over 50% TPP) are shown in Figure 13.4.1. A synergistic
effect is clearly seen when TPP is used with 2-5% salt; i.e, the combined effect of
NaCl and TPP is much greater than the simple additive effect of NaCl and TPP.
The “salting out” effect, previously discussed, is clearly seen at a salt level above
5%. Pyrophosphate and NaCl show an even greater synergistic effect compared
to TPP (Fig. 13.4.1) but pyrophosphates are not commonly used due to their
effect on pH and other factors. Hexametaphosphate, for example, results in higher
shrinkage during cooking. This raises the point that processors should know
exactly what kind of phosphate(s) or blend they are using but this is information
that some ingredient companies are not eager to share. However, with the new
Material Safety Data Sheet (MSDS) requirements, this information is becoming
easier to access by the meat processor.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-17
Fig 13.4.1
0
1
35
2
30 HMP 3
NO PHOSPHATES 4
25 TPP 5
KENA 6
% SHRINK
20 PP 7
8
15
9
10 10
0
0 1 2 3 4 5 6 7 8 9 10
% NaCl IN MEAT
Figure 13.4.1 Effect of NaCl on the shrinking of cooked chicken muscle (70°C) in the presence
of salt and different polyphosphates (0.5%). HMP – hexa meta phosphate; TPP – tri poly
phosphate; KENA – commercial phosphate blend; PP pyro phosphate (sodium acid).
Redrawn from Shults and Wierbicki (1973).
Most phosphates used by the meat industry help enhance the physical and sensory
properties of meat products by:
a. H elping extract the salt soluble proteins, hence increasing water holding
capacity and meat particle binding.
b. Shifting the pH away from the isoelectric point of the muscle’s proteins,
hence allowing more charges on the amino acid side chains. This can
result in increased repulsion between the proteins, which creates more
space for water molecules and more sites for water molecule binding.
c. Assisting in stabilizing meat emulsions due to the hydrophilic/
hydrophobic structure of the molecule
d. Slowing down oxidation due to the chelating effect of phosphate.
Certain phosphates can bind iron and other metals and prevent them from serving
as pro-oxidants. This helps extend the shelf life of the meat product in terms of
flavour but also protect it from meat pigment oxidation (colour problems).
FigureOxidation
Figure 13.4.3 13.4.2 The chemical
byproduct structure of sodium
values tri turkey
of raw polyphospate (STPP)Legends:
sausage. commonly used in meat
a) no additives ();
processing
b) (solubility
1.7% salt 14.5 ();
g in 100c)mlspice
at 25 C;only
pH of();
1% solution is 8.0).+From
d) spice Wikipedia.
rosemary Moree) spice +
();
detailed information
BHA/BHT (). Adapted from Material Safety Data
from Barbut Sheet
et al. can be found at:
(1985).
http://www.sciencelab.com/msds.php?msdsId=9927608.
Sodium ascorbate and sodium erythorbate (or their corresponding acids ascorbic
acid and erythorbic acid) are used at low concentrations of about 550 ppm. For
products that will be exposed to high temperature cooking (e.g., turkey/pork
bacon), a number of countries require that a curing accelerator be added as high
temperatures can increase nitrosoamine96formation (see previous discussion on
nitrite).
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-19
c. Spices – used to flavour and colour foods (e.g., paprika) as well as to add some
antimicrobial/antioxidant (e.g., rosemary) properties. In several cases they are
also used to enhance appearance (e.g., peppercorns on barbequed meat). Various
countries restrict the use of artificial food colouring in processed meat products,
hence the utility of spices for this purpose.
Examples of spices derived from different plant materials are listed below.
Large volumes of spice extracts, which contain essential oils and oleoresins
extracted from plant material, are sold to the meat industry. The oils can be obtained
by pressing, distilling, or solvent extraction, and they are usually concentrated to
obtain a more potent solution. The oils will be free of microorganisms if a high
distillation temperature or a strong solvent is used. Overall, the advantages of using
oil extracts include reduced transportation costs, long shelf life, and they do not
change the appearance of the product. In finely comminuted products such as hot
dogs and bologna, which have a very homogeneous appearance, this latter point
is very important (e.g., adding visible ground black pepper particles would not be
acceptable to the consumer). The extracts are usually highly concentrated and are
commonly sprayed on to a carrier such as salt or sugar (dextrose) in order to assure
an even distribution within the product.
Overall, natural and synthetic sugars vary in their sweetness. The standard for
the measurement is sucrose (a disaccharide composed of glucose and fructose
that comprises cane sugar), which is assigned a sweetness value of 100. On that
scale, dextrose (a monosaccharide of glucose) has a value of 74, fructose has a
value of 175, maltose (disaccharide of two glucose monomers) has a value of 40,
lactose (or milk sugar) has a value of 16, regular corn syrup solid has a value of
37 (therefore it can also be used as a partial bulking agent; see discussion below),
aspartame has a value of 180, and sucralose has a value of 600. There is a wide
selection of sugars to choose from and most commonly the meat industry uses
natural sugars at about 1 – 3 %. The reason for adding the sugar often determines
the type used. Reducing sugars contribute to the Maillard browning reaction when
they combine with secondary amines to form a brown pigment during heating.
Adding a reducing sugar such as dextrose, fructose, or maltose to a meat product
will enhance surface browning. This is important in smoked sausages where a
golden/brown colour is desirable (see recipe for smoked flavour turkey sausage at
the end of the chapter). Reducing sugars can be also added to fried products where
adequate golden/brown colour development during heating prevents overcooking/
burning the sausage.
The industry also uses synthetic antioxidants such as butylated hydroxy toluene
(BHT), butylated hydroxy anisole (BHA), and propyl gallate (PG). These
compounds are free radical terminators, as they have a cyclic carbon ring structure
that is capable of accepting a free radical molecule. These three compounds are fat
soluble and their usage level (where permitted) is commonly limited to 200 ppm
of the fat content. Figure 13.4.3 shows the beneficial effects of using a BHA/BHT
mixture (200 ppm) and natural rosemary oleoresin on delaying lipid oxidation
in a turkey sausage produced with 25% mechanically deboned meat, which is
highly susceptible to oxidation (see Chapter 9). Both the mixture and the rosemary
oleoresin were very effective in suppressing oxidation in the stored product. The
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-23
spice mix used in isolation also resulted in some antioxidant activity as compared
to the meat control treatment. Figure 13.4.3 also illustrates the effect of salt, which
can accelerate lipid oxidation due to a small amount of heavy metal (e.g., iron)
contamination. The data is reported as the amount of malonaldehyde (i.e. an
oxidation byproducts from the breakdown product of oxidized fatty acids), which
is commonly used in the literature to follow lipid oxidation. The publication also
lists the amounts of other byproducts (e.g., hexanal, heptanal, penanol; measured
by gas chromatography) that contribute to off odours that can be detected by a
sensory panel.
h. Mold inhibitors – are used to inhibit growth on the surface of dry and semi-dry
sausages that are not vacuum packed (molds are aerobic). This can be a problem as
these products have a water activity that supports mold (but not bacterial) growth.
Mold inhibitors are applied by dipping or spraying the outside casings. Common
chemical inhibitors include potassium sorbate and sorbic acid. These compounds
are permitted for use in some countries (e.g., USA), but not others (e.g, Canada).
In countries where these compounds are not permitted processors can use a cold
smoke treatment that contains natural antimicrobial compounds (see discussion
below) that help prevent mold growth.
i. Binders – are ingredients used to help bind meat particles and increase water
holding capacity (see also Section 13.5). These ingredients usually consist of
proteins that can form a gel system or participate in meat protein gelation. It is
obviously advantageous if they act synergistically with the meat proteins (see Fig
13.5.1, Aguilera and Kessler, 1989). These ingredients can be expensive so when
processors consider using them they should look for added values such as:
13-24 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
a. texture enhancement
b. water holding; i.e., reducing shrinkage during processing
c. improved product’s formulation
d. emulsification capabilities
e. reduction of formulation cost
The meat industry commonly uses dairy binders (e.g., milk powders and their
derivatives), vegetable proteins (soy, pea), and meat proteins (collagen, blood
plasma).
Soy proteins – commonly used as binders in products such as meat patties, meat
loaves, and sausages. In a number of countries their presence is limited to ≤ 2%
soy protein isolate or else the product name should include the word “soy”. Other
vegetable proteins such as pea are also used but to a lesser extent. The vegetable
proteins are also marketed under certain categories:
It should be noted that vegetable protein flours and grits usually have a distinct
flavour (beany) if used at a high concentration. Much work has been done over the
past decade to minimize this problem and today the standards for low beany off
flavours are much higher.
j. Fillers – are non-meat ingredients, usually made with complex sugars (e.g.,
starch) and low protein, that help bind water but not meat particles and are usually
considered to be good as bulking agents.
Fillers can be divided based on their cereal source (wheat, corn, starch) and are
added to the meat product either as flours or extruded/texturized particles. When
starch is heated past its gelatinization temperature in the presence of water it
opens up to bind water (e.g., can be 1:2 up to 1:10 ratio). At high temperatures the
solution becomes more viscous and when temperature is lowered (e.g., cooling
food/meat products after heating) the texture will become even more viscous. The
meat industry also uses pre-gelatinized starches where the starch manufacturer has
heated the product (in a solution) and then dried it. This creates a product that is
capable of binding water at lower temperatures, which is advantageous for the
meat industry because as meat proteins are heated (and denatured) they bind less
water. Please note that another popular application of flour and starches is in coated
products (see Chapter 14).
a. A
lginate – is extracted from brown algae (Phaeophyta) that is usually
harvested off the coasts of Ireland (Davis et al., 2003). Alginate is
composed of manmuronic and guluronic acid monomers; the ratio
between them determines the brittleness of the gel, water holding, etc.
Since the algae are harvested at different places and during different
seasons, there are variations in the gelling performance. Therefore, it
is important that the meat processor uses a supplier who is reputable
and can control and standardize the gel performance. One of the
unique characteristics of alginate is its ability to gel at room/refrigerated
temperature instantly when a small amount of calcium ions is added.
13-26 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
The meat industry uses it for binding raw meat particles in products such
as restructured cutlets (Fig. 13.4.4) in order to provide binding of the
smaller meat trimmings and hold the product together prior to cooking.
It isMeat
Figure 13.4.4 alsotrimmings
used today
boundtowith
make casingsgum
an alginate (Harper
to formeta al., 2013) that
restructured are co-
product. The
extruded
bindingdirectly
is done onto
at lowthe product (see
temperature withdiscussion
the help ofin Chapter
CaCl2 with10).
causes cold
gelation of the alginate. Showing a raw chicken and beef products, as well as the
resulting cooked beef product. Photo by S. Barbut.
Figure 13.4.4 Meat trimmings bound with an alginate gum to form a restructured product. The binding is
Figure
done at13.4.5 Carrageenan
low temperature gels
with the (1%)
help madewhich
of CaCl by the addition
causes of hot of
cold gelation water (85 °C)Showing
the alginate. followed
rawby
2
cooling
chicken and (see text
beef products, for as
as well explanation). The gel
the resulting cooked beefon the left
product. wasbymade
Photo from non-
S. Barbut.
refined carrageenan and the one on the right form refined carrageenan. The later
produced a clearer, harder, and more elastic gel, but with more syneresis. Photo
by S. Barbut.
arrageenan – gum that is extracted from Irish moss (Chondrus crispus
b. C
Stackh.) found along the Atlantic coast of the British Isles, Europe and
North America. It is composed of monomers of sulfated galactose
and anhydro-D-galactose. The gum is a complex mixture of about ten
different polymers. The main ones used by the meat industry are kappa
and iota (note: some lambda is also used to increase viscosity but it is a
non-gelling component). The type of gel formed depends on refining
the raw material (Fig. 13.4.5), the dominant polymer in the mixture and
the cation used to induce gelation during heating. Carrageenan forms a
reversible gel (i.e., can be remelted and reformed), is very effective at
binding water, and is added to products where water is used to replace
fat such as oven roasted turkey/chicken breast products and low fat
sausages.
97
Figure 13.4.5 Carrageenan gels (1%) made by the addition of hot water (85 °C) followed by
cooling (see text for explanation). The gel on the left was made from non-
refined carrageenan and the one on the right form refined carrageenan. The later
produced a clearer, harder, and more elastic gel, but with more syneresis. Photo
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-27
by S. Barbut.
Figure 13.4.5 Carrageenan gels (1%) made by the addition of hot water (85 °C) followed by
cooling (see text for explanation). The gel on the left was made from non-refined
carrageenan and the one on the right from refined carrageenan. The latter
produced a clearer, harder, and97more elastic gel, but with more
syneresis. Photo by S. Barbut.
c. X
anthan gum – is produced by microbial biosynthesis and is an
extracellular polysaccharide. It is composed of cellulose chains with
attached oligosaccharide groups. Low xanthan concentrations produce
a highly viscous solution. Together with locust bean gum, xanthan can
produce a thermo-reversible gel.
l. Acids/Acidulants – used to reduce pH, add flavour, extend the self-life and/or
produce a fermented-like meat product. A common example of an acid is vinegar
and an example of an acidulant is glucono delta lactone (GDL; introduced in the
1960s), which can yield a more rapid and improved colour development to cooked
comminuted meat products. An important advantage of using GDL is its slow
acid release that does not cause a problem with later protein binding (note: adding
a large amount of liquid acid to a meat product at the beginning of the process will
result in early protein denaturation, poor binding, and decreased WHC). Although
GDL was introduced to accelerate raw meat processing operations, it has been
later used in the production of fermented-like meat products (e.g., pepperoni for a
pizza topping and other industrial acidified products).
Encapsulated acids (e.g., lactic, citric) are another way to add acids to produce a
fermented-like products. The encapsulation material (wall component) is usually
made of hydrogenated vegetable oil with a melting point that has been adjusted
to be slightly higher than denaturation temperature for major meat proteins (e.g.,
13-28 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
m. Natural and Liquid Smoke – are mainly used to provide flavour, colour
(Maillard reaction), antimicrobial protection, and antioxidant compounds to the
surface of the product. Historically, smoking meat cuts over an open fire was
used to preserve different products. The exposure to mild/high temperature for an
extended period of time (e.g., several days; not currently used in the industry) also
resulted in significant drying. Today, smoking is commonly employed for a short
period of time (e.g., 10 - 90 min) and is mainly done to add flavour and colour and
to help increase the shelf life to the product.
There are several hundred different compounds in natural smoke. Maga (1989)
and Toledo (2007) reported over 300 in some of the commonly used hard woods
(maple, cherry). The compounds can be divided into four groups:
Smoke can be applied by burning the sawdust or pieces of hard woods (e.g.
maple, cherry) or as a liquid smoke solution. The former is achieved with the help
of a special generator outside the smokehouse. As the moist sawdust is slowly
burned, the smoke is circulated into the smokehouse by a fan system usually for
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-29
10 – 30 min. During this process, the exhaust duct must be closed so smoke can
accumulate and is not wasted. The product’s surface must be dry (it could be wet
due to condensate) or else the smoke will drip off. Liquid smoke is a newer product
that is prepared in dedicated facilities where smoke compounds from burning
wood are captured by letting the smoke rise inside a tall chimney equipped with
a counter flow water shower. The smoke compounds can later be concentrated
and the preparation is applied to meat products as a dip, spray, or atomized mist.
An advantage of this process is the ability to separate some/most of the polycyclic
hydrocarbons by allowing then to settle out. In addition, some liquid smoke
products can be added directly to the raw product after the pH has been adjusted.
The other major group of enzymes used is the one that can break down connective
tissue. Papain and ficin extracted from pineapples and figs respectively are able to
break down collagen and are sometimes used to tenderize meat. However, their
activity should be stopped at a certain point as extensive proteolysis can turn the
meat into mush.
Proteins are the main building blocks of meat products. Thus protein type (e.g.,
myofibrullar, sarcoplasmic, stromal proteins; see Chapter 3), configuration (Fig.
13.1.2), quantity, and quality (e.g., fresh vs. frozen) have major impact on the final
meat product characteristics. The product is also affected by processing parameters
such as the size of the meat pieces (small vs. large), addition of ingredients (e.g.,
salts, acidulants, gums), and cooking method (e.g., hot air vs frying). Overall, the
13-30 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
proteins interact with other components in the meat batter/product to form a gel
matrix. In any case, it should be recognized that proteins are the main functional
ingredient in meat products while the other two main components, water (30-
75%) and fat (5-30%), are important but do not directly contribute to structure
building. When discussing protein’s contribution to structure it is useful to look at
its interactions with the other components in the meat product:
Figure 13.5.1.a Possibilities for engineered structures of simple, mixed, filled and filled – mixed gels.
Figure 13.5.1.b Effect of filler type, from
Redrawn size, Aguilera
and volume fraction
and Kessler filler (φ) on the Young’s modulus
(1989).
(Ec) of particle-filled comminuted meat protein gels. (a,c) Rice bran wax;
strongly bound filler (insets show greater separation in the y-axis). (b,d) Glass
beads; weakly bound filler. Experimental data in (a) and (b) were fit to the
exactproduct
In general, a meat solutionisofcomposed
the van derofPoel modelsoluble
various (Eq. 2)and
and non-soluble
the Kerner model (Eq. 5),
proteins,
respectively. Fitted parameters are presented in the actual paper. The data
fat, water, andpresented
carbohydrates.
in (c) andTogether theytransformation
(d) is a ln-ln can form composite
of that shown materials that(b),
in (a) and
strengthen therespectively.
polymetric matrixNote: φdue
m in to volumetric
panels and/orthesurface
c and d denote volumephenomena.
fraction of theAgel
matrix. Particle size ranges ●: 1.0-1.4 mm, □: 0.50-0.60 mm, ▲: 0.15-0.21
non-food example is rubber, a polymer that can be described as a filled gel system.
mm, ◊: 0.045-0.090 mm, ▼: < 0.50 mm. From Gravelle et al. (2015).
When the so called carbon-black particles are added, there is a great increase in the
mechanical moduli. In such a case both the size of the carbon black particles and
their strong surface adsorption properties
98
contribute to the gel strength. Aguilera
and Kessler (1989) have also shown this strengthening phenomenon in a mixed
dairy gel containing small fat globules with modified membranes.
Gravelle et al. (2015) have reported on the physical and mechanical properties of
particle-filled composite gels prepared from chicken breast meat proteins. They
13-32 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
examined the effects of solid filler with varying size (1.0-1.4, 0.50-0.60, 0.15-0.21,
0.045-0.090, and < 0.50 mm) and surface properties (hydrophobic rice bran wax
particles and hydrophilic glass beads). All composites were found to be stable up to
0.5 volume fraction (φ) filler, based on post-gelation liquid loss, light microscopy
and cryo-SEM analyses. Both filler type and size were found to influence the
Young’s modulus and stress at 50% strain (Fig. 13.5.1.b). The recoverable
energy and post-compression height recovery were found to be predominantly
influenced by the filler volume fraction, and were less influenced by particle/gel
interactions. Interestingly, filler type and size range were observed to have no
effect on the cohesiveness of the composites, as this parameter was found to be
solely dependent on the volume fraction of the elastic filler present. The behavior
of the Young’s modulus was compared to that predicted by particle-reinforcement
theories proposed by van der Poel and Kerner, each with subsequent extensions
(Fig. 13.5.1 b).
Figure 13.5.2 Typical thermal curve of muscle with three major transition zones. Top figure
shows 13.5.1.b
Figure a summary of of
Effect denaturation peaks:
filler type, size, and (A) myosin
volume subunits;
fraction (B)onsarcoplasmic
filler (φ) proteins and
the Young’s modulus (Ec)
collagen (C) actin.
of particle-filled As muscle
comminuted type
meat and environment
protein change
gels. (a,c) Rice the shape
bran wax; ofbound
strongly the curve
filler changes
(insets
accordingly. Based on data from Barbut and Findlay (1989) and Wright et al. (1977).
show greater separation in the y-axis). (b,d) Glass beads; weakly bound filler. Experimental
data in (a) and (b) were fit to the exact solution of the van der Poel model and the Kerner
model, respectively. Fitted parameters are presented in the actual paper. The data pre-
sented in (c) and (d) is a ln-ln transformation of that shown in (a) and (b), respectively.
Note: φm in panels c and d denote the volume fraction of the gel matrix. Particle size
ranges ●: 1.0-1.4 mm, □: 0.50-0.60 mm, ▲: 0.15-0.21 mm, ◊:
0.045-0.090 mm, ▼: < 0.50 mm. From Gravelle et al. (2015).
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-33
Extrinsic factors are the environmental conditions surrounding the proteins and
include:
a. A mino acid composition – proteins that contain less than 31.5% mol
of hydrophobic residues (i.e., proline, leucine and tryptophan) form a
coagulum-type gel, whereas proteins with more than 31.5% hydrophobic
residues form a translucent gel. Some suggest that a more appropriate
parameter might be the ratio of the net charge to hydrophobicity rather
than hydrophobicity alone (Totosaus et al., 2002).
b. Electrostatic interactions – are related to the net charge of the protein
molecule as influenced by attractive and repulsive forces. They affect
protein–protein and protein–solvent interactions (Phillips et al., 1994).
These electrostatic interactions are promoted by changes in ionic strength
and/or pH (extrinsic factors).
c. Hydrophobicity – when non-polar amino acids are grouped together,
they form a hydrophobic nucleus surrounded by a polar residue layer
that remains in contact with the solvent (e.g., water). This plays an
important role in protein organization and should be taken into account
in any protein-folding consideration. Effective hydrophobicity refers
to the value representing the interactions between the proteins and
surrounding medium.
d. Molecular weight – differences in the average molecular weight and the
hydrodynamic size of polypeptide species could be related to variations
in the formation of self-supporting gel network and gel strength. The
polypeptide critical molecular weight for gel formation is about 23 000
Da.
e. Disulphide bonds and thiol-disulphide interchanges – increase the
apparent chain length of the polypeptide rather than acting as an initial
network stabilizer among polypeptide chains involved in protein
gelation. Disulphide bonds are not essential for gelation of proteins,
but their role in gelation is related to their ability to increase the average
molecular weight and hence the chain length.
Meat proteins denature at different temperatures (Fig. 13.5.2) and can then form
a gel structure. The figure shows that myosin and its subunits denature first (54-
58ºC), followed by sarcoplasmic proteins and collagen (65-67ºC), and then actin
as actomyosin and as fragments of F and G monomers denature last (71-83ºC;
Wright et al., 1977).
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-35
Figure 13.5.2 Typical thermal curve of muscle with three major transition zones. Figure
shows a summary of denaturation peaks: (A) myosin subunits; (B) sarcoplasmic
igure 13.5.3 Heat-induced gel
proteins andstrength of actomyosins
collagen (C) actin. reconstitution
As muscle type and environment change the of different myosin-t
ctin ratios. The protein samples
shape of the(5 mg/ml)
curve were dissolved
changes accordingly. in aBarbut
Based on data from 0.6 and
M KCl solution containi
Findlay (1989) and Wright et al. (1977).
0 mM phosphate buffer, pH 6, and incubated for 20 min at temperatures varying from 20 to
00C. Gel strength was measured at each temperature. M - myosin alone; A - actin alone; A
ctomyosin. TheStudying
figuresthein textural
parenthesis
changesindicate the mole
in a raw meat systemration
during (corrected) for myosin-to-ac
the cooking process
tio in respectiveand
systems.
correlatingFrom Yasui
that data et al. (1980).
with molecular changes is useful in understanding protein
gelation. As well, following the rheological changes (i.e., small deformation testing)
that take place during gel formation has been useful to studying the sequence of
molecular interactions within a food/meat system. The latter studies have become
more feasible within the last few years as the market has seen the development of
high precision programmable rheometers. Prior to the development of scanning
rigidity monitors, samples had to be changed for each temperature point, which
resulted in time being a continuous independent variable. An example of
information from an early thermal scanning rigidity monitor is shown in Figure
13.5.3. Yasui et al. (1980) studied the effect of using pure myosin, pure actin and
their combinations at different ratios on forming a gel matrix. The researchers
chose these two proteins because they are the main proteins responsible for meat
binding (i.e., myofibrillar salt-soluble proteins). Overall, binding characteristics
of meat products prepared from isolated myofibrillar proteins provide a basic
understanding of the gelation process. Figure 13.5.3 shows that myosin by itself
will start forming a gel at 45ºC. The authors indicated that this gel structure
determines the binding quality in meat products and that binding strength bears a
re 13.5.3 Heat-induced gel strength of actomyosins reconstitution of different myosin-to-
ratios. The protein samples (5 mg/ml) were dissolved in a 0.6 M KCl solution containing
13-36 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
mM phosphate buffer, pH 6, and incubated for 20 min at temperatures varying from 20 to
C. Gel strength was measured at each temperature. M - myosin alone; A - actin alone; AM
myosin. Theclose relationship
figures to the amount
in parenthesis of myosin
indicate liberated
the mole from
rationthe (corrected)
myofibrils. Thefor
datamyosin-to-actin
also show that actin by itself does
in respective systems. From Yasui et al. (1980). not form a gel under these conditions.
However, in the presence of myosin, a synergistic effect between actin and myosin
is observed. This is because actin, in the presence of other cross-linking proteins,
can enhance gel structure. The effect of the relationship between myosin and actin
concentration on rigidity is demonstrated in Figure 13.5.3. This can be used to also
illustrate the effect of a two protein system that produces a synergistic mixed gel
(see also Figure 13.5.1; second row on the right side). Maximum gel rigidity was
obtained when the myosin to actin mole ratio was 2.7, (a weight ratio of myosin
to actin of about 15:1). Increasing the portion of myosin beyond this point caused
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-37
a decrease in gel strength. Yasui et al. (1980) suggested that the synergistic effect
is either ionic strength dependent or is determined by the state of myosin per se
at different ionic conditions. At <40°C it can also be observed that actin exhibits
some resistance to gel, probably due to its thixotropic nature. However, upon
heating, the gel collapsed into a compact string or bead-like structure (scanning
electron microscopy pictures are not provided here). Isolated myosin fragments
were shown to affect gel characteristics differently. Intact myosin monomers
produced the strongest gels, followed by myosin rods and the S-1 fragment (see
Chapter 3 for myosin structure). The S-1 fragments produced gels with low
water-retaining ability. As mentioned above, the differences were also evaluated
by electron microscopy. Myosin rods produced an extended three-dimensional
network system, while the S-1 fragment formed a bead-like aggregate structure
upon heating. Combining the myosin rods and S-1 fragments did not produce high
gel strength as was observed for the intact myosin molecules. This indicates that,
once cleaved, the fragmented myosin did not have the same capabilities to form
a gel matrix.
Table 13.5.1 Effect of sodium chloride (NaCl), tripolyphosphate (TPP) and heating temperature on gel
strength and amount of extractable protein. Adapted from Barbut et al. (1996).
Structure development during heating of a commercial type meat batter can show
the direct relationship between the meat protein system (i.e., containing many
different proteins) and structure formation. Table 13.5.1 shows gel strength values
(measured via penetration force) for a chicken meat batter heated from 20-70ºC
and the available protein extracted at each temperature. As temperature increased,
more protein-protein interactions occurred and penetration force values increased
13-38 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
from 30 to 475N. At the same time the amount of available proteins decreased
because progressively more were bound together to form the gel structure. The
microstructure of the gels at the different heating temperatures is shown in Figure
13.5.4. As other researchers have shown, the basic gel structure is formed when
the meat batter is prepared (at low temperature) and is solidified during heating
through the creation of covalent and disulfide bonds.
In the study, Barbut et al. (1996) followed the gelation of finely comminuted
turkey meat (mechanically deboned) prepared with 13% fat and 2.5% NaCl and
in reduced sodium (1.5% NaCl plus 0.41% tripolyphosphate) products. From
20-70°C, the process was studied by evaluating gel strength, extracting available
proteins, and microscopy. Gel strength, as measured by the penetration test,
tripled as temperature increased from 50 to 55°C and then doubled again when
temperature was raised to 60°C (Table 13.5.1). The amount of extractable proteins
continuously decreased as heating temperature was raised. The decrease in the
amount of soluble protein indicates that they were taken up into the gel structure
(Asghar et al., 1985). Cryo-scanning electron micrographs (Fig. 13.5.4) revealed
that adding phosphate to the low sodium meat batter resulted in a protein matrix
with larger pores than the 2.5% NaCl treatment (both treatments were formulated
with equal ionic strength). The overall differences in microstructure of the two
treatments remained the same during cooking (micrographs taken every 10°C).
Development of a rigid gel structure during cooking was characterized by some
contraction of protein strands within the matrix. Closer examination of the data
revealed that the first major increase in rigidity was observed when the temperature
was increased from 20 to 40°C. This corresponded to an initial small reduction
in the amount of soluble protein (Table 13.5.1). A further increase was observed
from 40 to 50°C and then a major increase was observed when temperature was
increased from 50 to 55°C. The latter actually resulted in tripling gel strength values,
which could be related to myosin denaturation and its transformation into a rigid
structure. A major decrease in the amount of soluble protein at this range has been
previously reported by Yasui et al. (1980). They showed that, at this temperature,
interactions between actin and myosin were responsible for the rigid structure
development (i.e., actin by itself will not gel, but with myosin a synergistic effect
can be observed; Fig. 13.5.3). The values for gel strength were further increased
when the temperature was increased from 55 to 60°C. Temperature increases in
this range have been shown to be critical in the thermal gelation of meat systems.
The amount of extractable protein significantly decreased above 50°C in both the
2.5% salt and reduced salt treatments. This corresponded to the large increase
in gel strength. Contrast analysis showed that the overall means for extractable
protein were significantly different between the 2.5% NaCl and 1.5% NaCl + TPP
treatments across all temperatures.
igure 13.5.4 Cryo scanning electron micrographs of meat batters containing 2.5% NaCl (
strength = 0.42), heated to (A,B) 20 ºC; (C,D) 40 ºC; (E,F) 55 ºC; and (G,H
ºC. Micrographs on the left are at low magnification (bar = 15 µm), on the
at higher magnification (bar = 3 µm). Part G shows a fat globule entra
SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-39
within the proteinTHE
matrix. From Barbut et al. (1996). With permission.
101
13-40 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
polyphosphates were added to the reduced salt (1.5% NaCl) meat batters, structure
weakening around 63°C was eliminated; however, gelation patterns were different
depending on the phosphate. Adding 0.5% sodium acid pyrophosphate (SAPP)
resulted in the closest match to the rigidity modulus development pattern seen in
the 2.5% NaCl treatment. It is interesting to note that, in another study, a taste
panel also rated reduced-salt poultry frankfurters containing SAPP as having the
most closely matched texture to frankfurters containing 2.5% NaCl. The curve
of the TPP treatment shows that structure formation followed the pattern of the
1.5% NaCl treatment up to 64°C, but unlike the 1.5% NaCl, it did not weaken
and stayed at a constant value (G’=8.9) up to 80°C. Addition of SAPP resulted in
further increases of the G’ values as temperature was raised above 64°C. Evidently,
the change from a viscous to an elastic structure in a meat batter happens almost
instantaneously; additional heating further increases the rigidity modulus, but only
up to a certain point. It is important to note that salt and phosphate addition already
affect raw meat batter viscosity during preparation. This can be seen in Figure
13.5.5 as the differences in G’ at 20ºC. The authors also investigated the effects
of applying higher shear rates to the raw meat batters (Figure 13.5.6) in order to
determine viscosity and yield stress values. Both are important when selecting
pumps to move large volumes of meat in a processing plant.
Figure 13.5.5 Shear-rigidity modulus profile of reduced salt meat batters containing various
phosphates during heating. (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl +
0.5% TPP; 4=1.5% NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut
and Mittal (1989). With permission.
Figure 13.5.5 Shear-rigidity modulus profile of regular and reduced salt meat batters containing various
phosphates during heating. (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl + 0.5% TPP; 4=1.5%
NaCl + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut and Mittal (1989). With permission.
Figure 13.5.6 Relationships between shear stress and shear rate for reduced salt raw meat
batters with two phosphates (1 = 2.5% NaCl; 2 = 1.5% NaCl; 3 = 1.5% NaCl +
0.5%
13-42 CHAPTER 13:TPP; 4=1.5%
PRINCIPLES OF NaCl
MEAT + HMP; 5 = 1.5% NaCl + 0.5% SAPP). From Barbut
PROCESSING
and Mittal (1989). With permission.
The following short discussion is not directly related to meat protein gelation, but
is included here to explain flow behavior of raw meat batters and to help the reader
understand the forces involved. Figure 13.5.6 shows the relationship between
shear rate and shear stress for the same treatments shown in the previous figure.
The relationship is nonlinear and displays Bingham pseudo plastic behavior. The
shearing rate tends to increase faster than the shearing stress; i.e., also showing a
certain yield value. It was suggested that particles (e.g., muscle/connective tissue
fibers) in a meat batter are initially randomly oriented and become increasingly
more aligned as shear is applied. The contribution of particle interactions to the
apparent batter viscosity was reported to decrease when shearing stress increased.
All meat batters required the application of a certain shearing force before
any noticeable flow took place. On a molecular level, Bingham materials are
envisioned as a three-dimensional network at rest. Forces applied to this network
can be resisted up to a certain point, but then the network breaks down and the
flow becomes essentially pseudo plastic. Both NaCl treatments had the same pH
(6.35), TPP slightly increased the pH to 103
6.45, and SAPP addition decreased the
pH to 6.25. These relatively small pH differences are not believed to play a major
role in the viscosity differences observed. Rather, the type and concentration of
the salt ions involved seem to be most influential. The general power law model
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-43
(Herschel-Bulkley) with yield stress was used to fit the data. The 95% confidence
interval for yield stress (To) was 291 to 580 Pa, for the consistency coefficient (b)
was -11 to 191.0 Pa.sn, and for the flow behavior index (n) was 0.50 to 0.82. The
To for the emulsion containing 1.5 % NaCl + SAPP was significantly lower than
those of the other treatments. Thus, SAPP decreased the Bingham behavior of the
meat batter. Similarly, the To value for the control (2.5% NaC1) was significantly
higher than those of the other treatments. Thus, low NaCl (1.5%) reduced the To
value. The b value of the meat batters with 1.5% NaCl was significantly higher
than those of the 2.5% NaCl or 1.5% NaCl + phosphate batters. The n value was
between 0 and 1, indicating pseudoplasticity. Similarly, the n value of meat batters
containing 1.5% NaCl was significantly lower than those of other treatments.
According to previous work, more stable formulations tended to have higher b
values, lower n values, and larger values for yield stress. As indicated above, these
values and the relationships between them are important for equipment selection
in a meat processing plant.
The increase in G” was thought to be due to the partial unfolding of protein structure,
which caused an initial increase in the viscous characteristics of the SSPs. The
subsequent increase in G’, which indicated an increase in the elastic or solid nature
of the material, indicated that the SSPs were cross-linking to form an elastic gel.
An examination of the tangent delta (G”/G’) showed the relative viscous:elastic
properties of the material (i.e., in an elastic solid the tangent delta is zero and for a
viscous fluid it is infinite). For all pH levels, there were no significant differences in
13-44 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
the tangent delta values for the SSP preparations at the initial point prior to heating.
No second peak was observed in SSPs at pH 4.5, which corresponded to the lack
of transitions in both G’ and G”. Similarly, no significant differences in tangent
delta were observed at the first and second peaks in SSPs at 5.5, 6.5, and 7.5. At the
end point, protein gels at pH 4.5 showed higher viscous properties than at pH 6.5
and 7.5. This indicated that gels at pH 6.5 and 7.5 formed a more elastic network.
Table 13.5.2 Effect of pH on the storage modulus (G’), loss moduli (G”), and loss tangent
(tangent delta) of 3% chicken breast salt-soluble proteins heated from 30 to 80ºC at
1ºC/min and with 0.6 M NaCl. Adapted from Wang et al. (1990).
pH
Parameters
4.5 5.5 6.5 7.5
Storage modulus (Pa)
Initial point 34.2b 141.6ab 196.0a 187.0a
Peak maximum … 1,000.3 a
1,190.7 a
614.7a
End point 216.3b 1,725.7a 1,286.0a 575.9b
Loss modulus (Pa)
Initial point 6.8b 32.8ab 38.8a 31.4ab
Peak maximum … 116.6a 128.6a 82.8a
End point 24.4 b
123.1 a
30.6 b
24.9b
Loss tangent (temp;C)
Initial point
Temperature, C 30 30 30 30
Tangent delta 0.22a 0.23a 0.20a 0.17a
First peak
Temperature, C 37b 34c 47a 49a
Tangent delta 0.24a 0.20a 0.19a 0.17a
Second Peak
Temperature, C … 53b 57a 58a
Tangent delta … 0.15a 0.12a 0.15a
End point
Temperature, C 80 80 80 80
Tangent delta 0.12a 0.07ab 0.02b 0.04b
Means within the same row with no common superscripts are significantly
a,b
The authors also reported the complex modulus (G*, the amount of force required
to deform a sample). There were no major transitions at pH 4.5 when SSP
solutions were heated. This was because the proteins coagulated at this low pH
and did not from a gel network. This is typical of protein systems at pH levels
close to their isoelectric point (i.e., where the net charge on the proteins is close
to zero). The isoelectric point of actomyosin is around 5.0 and at this point an
electrostatic attraction between the molecules can be seen. Electrostatic attraction
minimizes protein unfolding during heating and prevents gel formation. At pH
5.5, 6.5 and 7.5, G* increased after the first transition at 35-47°C. Afterwards,
it peaked, then decreased on further heating to the third transition around 54-
60°C, and then increased again until 80°C. The first transition, which led to the
development of gel elasticity, was attributed to unfolding in the tail portion of the
myosin molecule. The G* values at the end of cooking were significantly higher
at pH 5.5 and 6.5 than at pH 4.5 and 7.5 (P < 0.05). The authors mentioned that
the thermal transitions, graphed as differential plots of the complex modulus
against temperature (dG*/dT versus T; not shown here), were pH-dependent
throughout the heating process. The differential plot illustrated the rate of G*
change during heating and provided additional information on how pH affects
protein conformational changes during sol-to-gel transition. No rate changes were
observed for the SSPs kept at pH 4.5 during the heating process. The first transition
of the pH 6.5 and 7.5 treatments occurred at temperatures above 45°C. At pH 5.5
even the third transition had occurred before any changes were observed in the
higher pH treatments. However, further transitions at pH 5.5 were similar to those
of the higher pH treatments; temperature differences between the first and sixth
transition were 18°C, 14°C, and 12°C for pH 5.5, 6.5, and 7.5, respectively. The
pH 6.5 and 7.5 treatments showed almost identical transition temperatures and
rheological transitions, which suggested similar changes in protein conformation
during the gelation process. These results also demonstrate that pH influences the
unfolding and aggregation of native protein molecules during heating and results
in different gel properties.
Overall, the data presented above indicate that pH should be monitored and
adjusted (if needed) to obtain consistent meat product quality. The texture and
water binding capacity of meat products can be manipulated by adjusting the pH
and by adding various salts and binders to optimize meat formulations.
13-46 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
From a practical standpoint, one of the major reasons for studying meat batter
stabilization is that during chopping the processor cannot see/detect any warning
signs indicative of a later “emulsion breakdown” (a term referring to fat separation
during cooking). This point is illustrated in Figure 13.6.1, which shows the effect of
chopping time on meat batter stability. As chopping time increases, more proteins
are extracted, fat particle size is reduced, and less liquid and fat is separated from
the product. This is known to most meat processors; however, just looking at the
raw meat batter usually does not provide any hint to the amount of liquid/fat losses
that can be expected during cooking. This is a constant challenge because meat
block formulations can change daily depending on the availability of raw materials,
cost, etc. Therefore, meat processors usually use pretty high safety margins (e.g.,
more proteins and longer chopping time; both of which increase processing costs)
to protect themselves against emulsion breakdown incidents. The data in Figure
13.6.1 are used to illustrate the point that understanding the process should benefit
the processor. This material was also used in the development of an automated
fiber-optic
Figure 13.6.1 Effect system to monitor
of chopping timethe
onemulsification
cooking lossprocess.
(ml) from comminuted beef meat batter.
Temperature values (ºC) at each time are listed above bars. From Barbut (1998).
There is still debate in the scientific community as to the correct definition of finely
comminuted meat products: meat emulsion or meat batter? The controversy arises
from the interpretation of the mechanisms responsible for holding the fat within the
13-48 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
The myofibrillar proteins, which have hydrophilic and hydrophobic sites, arrange
themselves in such a way that they reduce surface tension and forces responsible
for fat globule coalescence and prevent separation. The same phenomenon is
observed in homogenizing milk, where small fat globules are covered with the milk
protein caseinate (to help reduce fat separation/creaming). If finely comminuted
meat products hold fat using this mechanism, they would be considered true
emulsions. However, other researchers have suggested that the protein matrix is
the main factor responsible for physically entrapping the fat globules (Lee, 1985).
According to the physical entrapment theory, the viscous protein matrix restricts
fat globule movement, hence coalescence. This mechanism would suggest that
finely comminuted products are behaving as meat batters. In any case, the whole
issue of which mechanism is more important is not so simple, since numerous
changes take place during the production of products such as frankfurters/bologna.
During the initial stage of chopping, a flowable product, with a toothpaste-like
texture, is formed and the meat batter can be easily pumped (note: care should be
taken to limit shear forces, which can cause fat globules to coalesce and destabilize
the meat batter). The structure formed in the raw stage is shown in Figure 13.5.4.A.
Later, during the initial heating process (20-40ºC), the fat starts to melt and is
present in a liquid form. Myofibrillar protein denaturation and gelation starts at a
higher temperature (around 50ºC; see Fig. 13.5.4.E). At that point, the melted fat
starts to expand, collagen starts to be transformed into gelatin (i.e., liquid form),
and the salt soluble proteins form a gel. The texture of the product at the end of
the cooking process (70°C) is semi-rigid and does not flow anymore because the
salt soluble proteins have been denatured. As indicated above, there is continuing
debate about which mechanism is more important but today there is support for
the notion that fat stabilization is a combination of the ability of proteins to form an
interfacial film, as well as the formation of a gel matrix which physically restricts
the movement of fat globules prior to cooking (Youssef and Barbut, 2011).
The thickness of the interfacial protein film, its elasticity, complete or partial
coverage of the fat globules, and weak spots along the film have been discussed
by various researchers (Borchert et al., 1967; Jones and Mandigo, 1982; Barbut,
1999; Ramirez-Suarez and Xiong, 2003). The authors discussed the formation
of a relatively thin, flexible protein film around fat globules, and emphasized
the importance of pore formation as a “pressure release mechanism” during the
cooking stage (i.e., when fat is heated and expands). Some have experimentally
modified the thickness of the protein film by varying chopping procedures. Overall,
it appears that the formation of a relatively thin and flexible protein film provides
the best stability, whereas a thick inflexible film results in large ruptured holes
during cooking. Figure 13.6.3 illustrates the microstructure of stable and unstable
finely comminuted meat products. In the stable product, fat globules are confined
within a distinct globular structure. In the unstable product (in this figure caused
13-50 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
by Tween 80 addition) they are distorted in shape and start to form fat channels.
Destabilization can also be caused by decreasing the salt level (e.g., 2.5 to 1.5%),
which is associated with lower protein extractability and subsequently higher fat
and moisture losses during cooking (Acton et al., 1983). The combined loss of
fat and moisture from finely comminuted meat products has been mentioned by
Schmidt (1984), who observed that fat exudation usually follows moisture loss.
Schmidt postulated that the formation of channels through the meat batter was
important to allow some moisture and fat losses. Figure 13.6.2 shows a fat globule
that has lost some of its fat, during cooking, due to salt reduction in the raw meat
formulation (2.5 to 1.5%). The scanning electron micrograph reveals a protein
envelope around the fat globule. When too much fat is exuded from the globule, the
protein envelope shrinks and indentations plus small exudative holes are seen on
the surface. When salt is increased, little or no fat is lost and round globules can be
seen. Whiting (1987) has also reported that 1.5% salt is a threshold in frankfurters,
as determined by the amount of fat and water released during cooking. It should be
mentioned that the amount of salt required to produce a stable batter also depends
on factors such as the amount of fat and protein and their quality.
The connection between the texture of the meat protein matrix and the size of the fat
globules can be seen in Table 13.6.1. Youssef et al. (2011) indicated that increasing
the meat protein level (9–15%) increased the hardness of finely comminuted meat
batters prepared with beef and animal fat or canola oil (CO). Overall, a higher
protein level formed a denser protein network (microstructure not shown here),
which had increased resistance to compression. The meat emulsions prepared with
animal fat showed lower fracturability and hardness values compared to the CO
emulsions. This is most probably due to the higher number of small CO globules
present in a given volume (similar results were also shown for milk protein gels).
In a previous experiment the authors showed that fat globule size was reduced
from 6627 to 121 μm2 when beef fat was substituted with CO at 8% protein. The
same idea can also be seen here in Figure 13.6.3. Overall, the presence of smaller
fat globules and higher protein increase resistance to compression. This is in line
with the composite gels discussed at the beginning of the section.
The treatments with Tween 80 + animal fat resulted in higher fat and moisture
losses than the CO-Tween 80 or animal fat treatments (Table 13.6.1). This resulted
in an increased protein concentration and higher hardness values in the cooked
products; i.e. they formed denser protein matrixes.
Table 13.6.1 Effects of meat protein level and fat type on texture profile analysis parameters of cooked finely comminuted meat batters Meat batters were produced with 9, 12 or
15% protein, with either beef fat (BF), or canola oil (CO; all treatments contain 25% fat or oil). An emulsifier (Tween 80 indicated as T-80) was added to one set of products,
and sodium caseinate (SC) was used to replace 2% of the meat proteins in another set. M=meat protein; P*=indicates total protein when 2% SC was used.
Data adapted from Youssef et al. (2011).
a-p
Means within a column no common superscript are significantly different (P < 0.05).
13-51
13-52 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
The CO-T80 batters had lower hardness values than batters prepared with CO,
possibly related to the formation of an incoherent protein matrix (Fig. 13.6.3).
When Tween 80 surrounds fat globules it can interfere with the interaction of the
interfacial protein film with the actual protein matrix. Theno and Schmidt (1978)
observed that fat particles coated with proteinaceous material could cross link with
the protein matrix and therefore stabilize frankfurters. It was suggested that the
physical binding
Figure 13.6.3 Lightofmicrographs
fat might be the result
of meat battersof protein–protein
with interactions
pre-emulsified fat/oil between
with T-80. Fat
the interfacial protein film and the matrix proteins.
globule (FG); Meat protein (MP); canola oil (CO) made with beef fat (BF); pre-
emulsified with Tween 80 (T80) or with the addition of sodium caseinate (SC).
Bar = 200µm. From Youssef et al. (2011). With permission.
Figure 13.6.3 Light micrographs of meat batters with pre-emulsified fat/oil with T-80. Fat globule
(FG); meat protein (MP); made with canola oil (CO), or beef fat (BF); pre-emulsified with Tween
80 (T80) or with the addition of sodium caseinate (SC). Bar = 200µm.
From Youssef et al. (2011). With permission.
The use of sodium caseinate (SC), which is used by the meat industry to stabilize
fat, lowered fracture and hardness values at the 9% protein level (hardness of 12.48
vs. 17.13 N with and without SC, respectively) when 2% of meat proteins were
replaced with SC. This was because SC cannot form a heat induced gel (at 72°C)
and the amount of meat protein (7%) was insufficient to produce a hard texture.
However, when 12% protein and 2% SC was used, the texture was comparable to
the 12% meat protein. At 15% protein105 (13% meat protein and 2% SC), hardness
surpassed the control (15% meat proteins). CO-SC batters showed reduction in
hardness values at the 9% and 12% protein levels compared to the comparable CO
treatments. This change in hardness indicates that incorporation of pre-emulsified
fat/oil with SC can significantly modify the textural properties of meat batters.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-53
Replacing beef fat with CO also increased springiness and cohesiveness; this
is possibly related to the size and distribution of the fat globules (Table 13.6.1),
which agrees with previously published data.
Overall, the control beef fat treatment revealed a typical meat batter in which
fat globules are embedded within a homogenous protein matrix (Fig. 13.6.3).
Microstructure was affected by the type of fat/oil and protein content. In all
treatments, increasing protein resulted in the formation of a denser protein matrix
structure, caused by the higher amount of extracted salt soluble proteins forming
more protein–protein interactions. Replacing beef fat with CO showed a larger
number of small, closely packed, fat globules compared to the beef fat treatment.
This is because of the liquid nature of CO relative to the more solid nature of
beef fat, which plays an important role during chopping. As meat protein level
was raised in the CO emulsions, irregularly shape fat globules began to appear
as fat globules coalesced into larger globules that later led to the formation of fat
channels. The discontinuity of the protein matrix allowed fat and liquid to leach
out of the matrix.
The beef fat -Tween 80 (BF - T80) showed more protein matrix aggregation
than the beef fat treatment, suggesting that fat mobility overcame the ability of
the protein matrix to contain the fat. This resulted in large irregularly shaped and
elongated fat pools; this also caused meat batter instability (Fig. 13.6.3). The CO-
Tween 80 treatment, at 9% protein, showed an incoherent matrix with very few fat
globules with visible IPF. In the past, non-protein emulsifiers, particularly Tween
80, were shown to be preferentially absorbed by fat globules than meat proteins
because of their higher hydrophilic–lipophilic balance values. This can reduce
protein–lipid interactions by interfering with the adsorption of protein molecules
to the fat globule surfaces and can result in decreased binding of fat globules to the
protein matrix.
Figure 13.6.4 Means of fat and 106fluid losses of meat batters prepared with 25% beef fat (BF) or canola
oil (CO) and pre-emulsified fat/oil with T-80 or sodium caseinate (SC) at different protein levels. All
treatments contain 25% fat or oil; 2% of the meat protein was substituted with SC; M, meat protein;
BF-T80, beef fat pre-emulsified with T-80; CO-T80, CO pre-emulsified with T-80; P, protein;
BF-SC, beef fat pre-emulsified with SC; CO-SC, CO pre-emulsified with SC. Means related
to fluid loss (r-z), and fat loss (a-f), with no common superscript are significantly different
(P < 0.05). Last six treatments; 2% of the meat proteins (M) were substituted with SC and
then denoted as P* to show total protein in the whole treatment.
From Youssef et al. (2011). With permission.
13.7 Casings
Meat and sausages have been stuffed into natural casings for thousands of years.
Today this continues in the industry but with increased automation, a larger variety
of pre-formed casings (Fig. 13.7.1), and the option for co-extrusion. The latter has
been one of the most significant developments in sausage casings over the past
century. This process allows continuous, direct deposit of an initially semi-liquid
material (e.g., collagen paste) onto the product as it is extruded from the stuffer.
This has allowed the industry to move from a batch type operation to a continuous
operation (see also Chapter 1 discussing automation). The continuous operation is
a key concept in reducing labour cost, increasing efficiency, and introducing more
mechanization into the process. However, it should be pointed out that the process
does not fit all products (e.g., large diameter sausages) and the initial capital cost
can be high.
Figure 13.7.1 Different typesTHE
of SCIENCE
casings OF
used for various
POULTRY meat PROCESSING
AND MEAT products. Products
– BARBUTmade at the
13-55
University of Guelph. Photo by S. Barbut.
Figure 13.7.1 Different types of casings used for various meat products.
Products made at the University of Guelph. Photo by S. Barbut.
When producing a sausage, the raw meat batter consists of ground/chopped meat
which is a fairly viscous material that can be pumped and stuffed into different sized
casings. During cooking, the meat proteins are denatured and form a heat stable
gel (see Section 13.5). At that point, the cooked firm product can be removed from
the casings (e.g., cellulose casings stripped off hot dogs at the meat plant), or by
the consumer prior to slicing/consumption (e.g., salami casings removed at home
by the consumer). In the case of edible casings (natural or manufactured collagen)
the casing is left on the product (see recipe for European Style Chicken Weiners at
the end of the chapter).
As mentioned above, humans have been using natural casings, such as those
derived from the gastrointestinal tracts of sheep, cattle, etc., for thousands of
years. These casings are still popular in certain products and to some represent
the golden standard. Over the past century, there has been a rapid development of
new packaging materials, including casings (Savić and Savić, 2002), and currently
there are hundreds of different casings on the market. Overall, they can be divided
into a few groups based on their origin.
a. Natural collagen casings are derived from the digestive tracts of sheep and
107encephalopathy (BSE) problem, cattle
hogs. Because of the bovine spongiform
13-56 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
different thicknesses and degrees of cross linking. They are made at special plants
and cross linking agents such as ammonia or gluteraldehyde can be used as well
as special colouring agents. Their microbial counts are much lower than natural
casings since they are manufactured from collagen that was extracted at high pH.
Like natural casings they are permeable to water and smoke and can also adhere to
the product and shrink with it.
c. Co-extruded casings are made from pretty much the same material as the
manufactured casings described above and are often made by the same companies.
The collagen gel is usually sold to the industry as a 3.5 – 5.5% protein dough. It is
used by the meat processor with a special counter rotating head (see Chapter 10
for description of the equipment) that dispenses the gel on top of the product while
it is coming out of the stuffer. Later on, the casing is dewatered to some extent in a
salt bath, dried in an oven, and the collagen molecules are cross-linked with liquid
smoke (i.e., using the aldehyde components; see discussion on liquid smoke in this
chapter). This is usually followed by a full cook cycle inside or outside a cook-in-
bag. Note that there is also a process where alginate is used for co-extrusion but
the sensory characteristics are different compared to collagen casings. New hybrid
gels of collagen and alginate have also started to appear on the market (Harper et
al., 2013).
111
13-60 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
112
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-61
113
Figure 13.7.3 Light micrographs of cellulose and plastic casings. First frame
shows: (1a) and (1b) thin cellulose type “Fast-peel”; (1c) and (1d) large dia-
meter regular casings covering the actual meat batter; (1e) and (1f) outside
polyvinylidene dichloride (PVDC) coated cellulose casings; (1g) and (1h)
inside PVDC coated cellulose. Polarized light was used in (1b), (1d), (1f),
and (1h) to reveal cellulose fibers. Bar = 200 μm. Second frame shows:
(2a) and (2b) fibrous/cotton casing covering a meat batter; (2c) and (2d)
outside coated fibrous/cotton; (2e) and (2f) extruded plastic casing. Pol-
arized light was used in (2b), (2d) and (2f) to reveal cellulose fibers/
special plastic. Bar = 200 μm. Third frame shows scanning electron
micrographs of casings: (3a) thin cellulose type “Fast-peel”; (3b)
large diameter cellulose sausage; (3c) outside PVDC coated
cellulose; (3d) inside PVDCcoated cellulose; (3e) regular
fibrous/cotton; (3f) outside coated fibrous/cotton; 3(g)
extruded plastic; and (3h) lower magnification of
micrograph “f” - see box. Bars = 25 μm for all,
except (3h) which is 120 μm. From Barbut
(2011). With permission.
13-62 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
e. Plastic polymer casings are very popular for water/steam cooked sausages
because they are impermeable to water (this is advantageous as water is a more
efficient medium to transfer heat than dry, hot air). A simple way to demonstrate this
is by imagining putting your hand into an oven set at 100ºC compared to a boiling
pot of water. Where smoking and drying of the sausage surface is not required,
plastic casings represent a viable option. The microstructure of a plastic casing can
be seen in Figure 13.7.3 and a product in this casing is shown in Figure 13.7.4.
The micrograph shows the lamination of the layers and is basically a dense barrier.
Extruded plastic casings are strong and uniform, and can therefore be used for very
large diameter products. They also offer protection against oxidation since they
are usually impermeable to oxygen. This also means that they are impermeable to
smoke. Thus, if smoke flavourings are desired they should be added to the meat
mix. There are also some new developments where liquid smoke can be applied
to the inside of the casings prior to stuffing. Materials such as polyethylene, nylon
and polypropylene are used as a single layer or as a combination of different layers
in the manufacture of plastic polymer casings (Savić and Savić, 2002). These
casings are extruded so usually there is no seam/weak point in the casing. The
casings can be coloured and material printed on them can be used to describe the
product (e.g., nutritional label). Casings can also be extruded with a UV-barrier so
colour fading is not a problem (see Chapter 16).
Figure 13.7.4 Plastic casings used for a jelly meat loaf. Photo by Barbut.
Figure 13.7.4 Plastic casings used for a jelly meat loaf. Product made at the University of Guelph.
Photo by
Figure 13.8.1.1 Oven roasted chicken. Photo byBarbut.
Barbut and Jinde.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-63
f. Metal casings/molds are commonly used for canned meats (e.g., meat
loaf processed at high temperature, 121ºC, in hermetically sealed cans) or for
producing large sausages/hams/loaves at lower temperature (70 - 80ºC). The
mold provides the product with a certain defined shape. This is important for large
meat masses and it also helps in precise portion control when using high speed
automated systems. In some cases, a cellulose or plastic casing is used to stuff
the product before it is placed in a metal press to facilitate removal of the cooked
product (no sticking and/or peeling surfaces) and cleaning of the molds. When
plastic casings are used, prior to placing the meat in the mold, they are often left
on the product after cooking and act as the packaging material that also provides a
barrier against cross/re-contamination of the product. This technology can be seen
in the preparation of oven roasted turkey breast, 4 × 4 hams, etc.
g. Retortable pouches are flexible pouches usually made from several layers of
synthetic polymers, of which aluminum foil is one. They provide good moisture
and oxygen barrier properties. It is interesting to note that although the pouch
thickness appears small, it can contain a dozen different layers. The pouches can
be used for meat products that are sterilized at high temperatures. Slices of meat
loaf-type products and chicken soup/stew are commonly packaged in such a
way and then retorted at a temperature of about 121ºC. The advantage of these
thin pouches is that they can reach the desired cooking temperature much faster
than a traditional round can. As with cans, the product is shelf stable after the heat
treatment and no refrigeration is needed.
13.8 Formulations
In this section you will find various recipes of further processed meat products
popular around the world. The recipes are courtesy of Hermann Laue Spice
Company, Canada. These formulations are used by the industry but here they only
serve as general guidelines and should be used as such. Also, local government
regulations vary among countries (e.g., use of additives such as nitrite, phosphate)
and therefore careful examination of local legislation is required. The section
13-64 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Ingredients
Meat:
Brine:
• 20.0 kg
Processing
114
Ingredients
Meat:
Brine:
• 30.0 kg
Processing
Ingredients
Processing
Ingredients 115
Meat:
Brine:
• 15.0 kg
Processing
Ingredients
Meat:
Brine:
• 20.0 kg
Processing
Ingredients
Meat:
Brine:
• 40 kg
• 28 kg cold water
• 6.5 kg ice
• 5.5 kg brine and cure unit
• (salt, soy/whey proteins, phosphate, spices, erythorbate, nitrite)
13-70 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Processing
• L acerate the turkey thigh meat (especially from the skin side) to increase
the surface area.
• Tumble the meat with the brine in a well-chilled vacuum tumbler for 6
hr at 12-15 rpm.
• Rest overnight and tumble for 1.5 hr the next day.
• Stuff the meat into cook-in-bags (also referred to as “cook & ship bags”).
• Place hams into 4 × 6 inches ham molds and press firmly.
• Cook in a smoke house by using steam at a temperature of 78°C, until
reaching an internal temperature of 71°C (Fig. 13.8.6.1).
• Shower with cold water to chill quickly prior to transferring to a
refrigerator.
Ingredients
Meat:
• 50 kg
Processing
Ingredients
Processing
Ingredients
Processing
Ingredients
Meat:
• 16.0 kg salt
• 5.0 kg Tikka Masala seasoning unit
• 1.0 kg potato starch
• 0.2 kg phosphate
Processing
• M ix the ground chicken meat with all the ingredients until a good bind
has developed.
• Add the water in 2-3 steps while mixing.
• Stuff the meat batter into collagen casings of desired caliber, link to the
desired weight and pack. Product to be kept refrigerated or frozen prior
to shipping.
Ingredients
Spice ingredients:
• 1.9 kg salt
• 0.9 kg kielbasa seasoning
• 0.8 kg brown sugar
• 0.6 kg curing salt (includes erythorbate and nitrite)
• 0.3 kg phosphate
Processing
116
13-76 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Ingredients
Meat:
Ice:
• 28.0 kg
• 1.7 kg salt
• 1.4 kg dextrose
• 1.0 kg modified starch
• 0.8 kg Wiener seasoning
• 0.6 kg curing salt (with erythorbate and nitrite)
• 0.2 kg phosphate
• 0.1 kg paprika
• 0.1 kg onion powder
Processing
Ingredients
Meat:
Ice:
• 14.0 kg
Processing
• S lowly cut the slightly frozen meat with about 5 kg of flaked ice in a
bowl chopper for a few revolutions.
• Add the binder unit, salt and phosphate and chop at the high speed setting
while adding the rest of the ice until temperature reaches 8-10°C.
13-78 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Ingredients
Meat:
Water:
• 1.7 kg salt
• 1.5 kg mild pepperoni seasoning
• 1.5 kg potato starch
• 1.2 kg liquid vinegar
• 1.0 kg corn syrup solids
• 0.6 kg curing salt (including erythorbate and nitrite)
• 0.3 kg phosphate
Processing
Ingredients
Meat:
Processing
• M ix all of the ground meat and fat together with the spices and cure until
a good bind has developed.
• Stuff the batter into natural casings or collagen casings (calibre 15-20
mm).
• Process the product in a smokehouse:
• Dry heat at 55°C for 2 hr.
• Dry heat at 60°C for 1 hr.
• Dry heat at 65°C for 1 hr.
• Dry heat at 72°C for 1 hr or until the desired dryness is reached.
• If desired, hot smoke can be applied during the second drying cycle.
• Product to be air cooled only.
Ingredients
Meat:
Water:
• 10.0 kg (cold)
Figure 13.8.14.1 Turkey pepperoni sticks. Photo by Barbut and Jinde.
THE SCIENCE OF POULTRY AND MEAT PROCESSING – BARBUT 13-81
Spice:
Processing
Ingredients
Meat:
Water:
• 5.0 kg (cold)
Spice:
Processing
Ingredients
Meat:
Water:
• 15.0 kg (cold)
Spice:
Processing
• N
ote: other variations, such as Hot Buffalo Chicken Wings can also be
made the same way, but with a different spice mix.
• Keep product refrigerated or frozen prior to shipping.
Ingredients
Meat:
Water:
• 5.0 kg (cold)
Spice:
Processing
• Place the well chilled fresh chicken drum sticks into a vacuum tumbler.
• Dissolve the dry ingredients in the cold water and vacuum tumble for
15 – 20 min.
• Remove the seasoned chicken drum sticks from the tumbler, tray pack
and overwrap.
Ingredients
Meat:
Spice:
Processing
Ingredients
Meat:
Vegetables:
Gelatin:
Processing
• A
dd the proper amount of gelatin solution into the casings and remove
all air bubbles prior to clipping.
• Cool down in a cold water bath (see Fig 13.7.4).
Ingredients
Meat:
Vegetables:
Spice:
Processing
See Chapter 14
13-86 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
References
Aberle, E.D., J.C. Forrest, D.E. Gerrard and E.W. Mills. 2012. Principles of Meat
Science. Kendall/Hunt Publ., Dubuque, IA.
Acton, J.C., G.R. Ziegler and D.L. Burge. 1983. Functionality of muscle
constituents in the processing of comminuted meat products. CRC Rev.
Food Sci. Nutr. 18:99.
Aguilera, J.M. and H.J. Kessler. 1989. Properties of mixed and filled type dairy
gels. J. Food Sci. 54:1213.
Barbut, S. 1998. Use of fiber optic probe to predict meat emulsion breakdown.
Ital. J. Food Sci. 10:253.
Barbut, S., D.B. Josephson and A.J. Maurer. 1985. Antioxidant properties of
rosemary oleoresin in turkey sausage. J. Food. Sci. 50:1356.
Borchert, L.L., M.L. Greaser, J.C. Bard, R.G. Cassens and E.J. Briskey. 1967.
Electron microscopy of a meat emulsion. J. Food Sci. 32:419.
Cassens, R.G. 1990. Nitrite- Cured Meat: A Food Safety Issue in Perspective.
Food Sci. and Nutr. Press. Trumbull, CN.
Foegeding, E.A., E.L. Bowland and C.C. Harding. 1995. Factors that determine
the fracture properties of globular protein gels. Food Hydrocolloids 9:237.
Gravelle, A.J., A.G. Marangoni and S. Barbut. 2015. Influence of particle size
and interfacial interactions on the physical and mechanical properties of
particle-filled myofibrillar protein gels. Royal Soc. Chem. Adv. 5:60723.
Jones, K.W. and R.W. Mandigo. 1982. Effect of chopping temperature on the
microstructure of meat emulsions. J. Food Sci. 47:1930.
Harper, B.A, S. Barbut, L.T. Lim and M.T. Marcone. 2013. Characteristics
of ‘wet’ alginate and composite films containing gelatin, whey and soy
proteins. Food Res. Int. 52:452.
LaBudde, R.A. and T.C. Lanier. 1995. Protein functionality and development
of bind values. In: Proc. Reciprocal Meat Conference, San Antonio, TX.
48:59.
Maga,J.A. 1989. Smoke in Food Processing. CRC Press, Boca Raton, FL.
13-88 CHAPTER 13: PRINCIPLES OF MEAT PROCESSING
Montejano, J.G., D.D. Hamann and T.C. Lanier. 1984. Thermally induced
gelation of selected comminuted muscle systems - rheological changes
during processing; final strengths and microstructures. J. Food Sci. 49:1496.
Pearson, A.M. and F.W. Tauber. 1984. Processed Meats. AVI Publ., Wesport,
CT.
Prakash, A., S. Sen and R. Dixit. 2013. The emerging usage and applications of
nanotechnology in food processing industries: the new age of nanofood. Int.
J. Pharm. Sci. Rev. Res. 22(1).
Savić, Z. and Savić, I. 2002. Sausage Casings. p.354. Victus Inc., Vienna, Austria.
Sebranek, J.G. and J.N. Bacus. 2007. Cured meat products without direct addition
of nitrate or nitrite: what are the issues? Meat Sci. 77(1):136.
Shults, G.W. and E. Wierbicki. 1973. Effects of sodium chloride and condensed
phosphates on water holding capacity, pH and swelling of chicken muscle.
J. Food Sci. 38:991.
Sindelar, J.J. and A.L. Milkowski. 2012. Human safety controversies surrounding
nitrate and nitrite in the diet. Nitric Oxide. 26(4):259.
Toledo, R.T. 2007. Wood Smoke Components and Functional Properties. In:
International Smoked Seafood Conference Proceedings. Kramer, D.E. and
L. Brown (Eds). Alaska, USA, p55.
Totosaus, A., J.G. Montejano, J.A. Salazar and I. Guerrero. 2002. A review of
physical and chemical protein-gel induction. Int. J. Food Sci Tech. 37:589.
Wang, S.F., D.M. Smith and J.F. Steffe. 1990. Effect of pH on the dynamic
rheological properties of chicken breast salt-soluble proteins during heat-
induced gelation. Poultr. Sci. 69:2220.
Whiting, R.C. 1987. Influence of various salts and water soluble compounds on
the water and fat exudation and gel strength of meat batters. J. Food Sci.
52:1130.
Wright, D.J., I.B. Leach and P. Wilding. 1977. Differential scanning calorimetric
studies of muscle and its constituent proteins. J. Sci. Food Agric. 28(6):557.
Xiong, Y.L. and C.J. Brekke. 1991. Protein extractability and thermally induced
gelation properties of myofibrils isolated from pre- and post-rigor chicken
muscles. J. Food Sci. 56:210.
Youssef, M.K., S. Barbut and A. Smith. 2011. Effects of pre emulsifying fat/
oil on meat batter stability, texture and microstructure. Int. J. Food Sci.
Technol. 46(6):1216.
Youssef, M.K. and S. Barbut. 2011. Effects of two types of soy protein isolates,
native and preheated whey protein isolates on emulsified meat batters
prepared at different protein levels. Meat Sci. 87(1):54.